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Nicking activity on pBR322 DNA of ribosome inactivating proteins from Phytolacca dioica L. leaves

Identifieur interne : 002F75 ( Main/Exploration ); précédent : 002F74; suivant : 002F76

Nicking activity on pBR322 DNA of ribosome inactivating proteins from Phytolacca dioica L. leaves

Auteurs : Serena Aceto [Italie] ; Antimo Di Maro [Italie] ; Barbara Conforto [Italie] ; Gesualdo G. Siniscalco [Italie] ; Augusto Parente [Italie] ; Pasquale Delli Bovi [Italie] ; Luciano Gaudio [Italie]

Source :

Biological Chemistry [ 1431-6730 ] ; 2005.

RBID : ISTEX:28A25948CEDC81A8E69393A3C4ABC86F3081B5F0

English descriptors

Teeft :
- Agarose, Amersham biosciences, Bamhi, Barbieri, Biochem, Cleavage, Cleavage site, Clone, Coli, Competent cells, Deletion, Dephosphorylated, Digestion, Dioica, Dioicin, Divalent, Divalent cations, Divalent metal ions, Dnase, Ecori, Edta, Endonuclease, Endonucleolytic, Endonucleolytic activity, Experimental conditions, Feb, Febs lett, Final reaction products, Incubation time, Ionic strength, Klenow fragment, Labelling experiments, Lett, Ligated, Linear form, Linearisation, Linearised, Molecular weight, Mung bean nuclease, Mutant clones, Nacl, Nicking, Nicking activity, Nuclease, Nucleic, Nucleic acids, Phytolacca, Phytolacca dioica, Plasmid, Pmol, Preferential cleavage site, Proof nicking, Psti, Purification procedure, Restriction endonucleases ecori, Restriction enzymes, Ribosome, Rip, Rrna, Same conditions, Standard conditions, Stirpe, Supercoiled, Supercoiled forms, Zn2q.

Abstract

Ribosome-inactivating proteins isolated from Phytolacca dioica L. leaves are rRNA-N-glycosidases, as well as adenine polynucleotide glycosylases. Here we report that some of them cleave supercoiled pBR322 dsDNA, generating relaxed and linear molecules. PD-L1, the glycosylated major form isolated from the winter leaves of adult P. dioica plants, produces both free 3′-OH and 5′-P termini randomly distributed along the DNA molecule, as suggested by labelling experiments with [α-32P]dCTP and [γ-32P]dATP. Moreover, when the reaction is carried out under low-salt conditions, cleavage is observed mainly at a specific site, located downstream of the ampicillin resistance gene (close to position 3200), ending with the deletion of a fragment of approximately 70 nucleotides. This cleavage pattern is similar to that obtained under the same conditions with mung bean nuclease, a single-strand endonuclease. Furthermore, pBR322 DNA treated with PD-L1 shows reduced transforming activity with E. coli HB101 competent cells in comparison to untreated control plasmid DNA.

Url:

https://api.istex.fr/ark:/67375/QT4-PQ1KK8CQ-5/fulltext.pdf

DOI: 10.1515/BC.2005.037

Affiliations:

Italie

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Le document en format XML

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<term>Amersham biosciences</term>
<term>Bamhi</term>
<term>Barbieri</term>
<term>Biochem</term>
<term>Cleavage</term>
<term>Cleavage site</term>
<term>Clone</term>
<term>Coli</term>
<term>Competent cells</term>
<term>Deletion</term>
<term>Dephosphorylated</term>
<term>Digestion</term>
<term>Dioica</term>
<term>Dioicin</term>
<term>Divalent</term>
<term>Divalent cations</term>
<term>Divalent metal ions</term>
<term>Dnase</term>
<term>Ecori</term>
<term>Edta</term>
<term>Endonuclease</term>
<term>Endonucleolytic</term>
<term>Endonucleolytic activity</term>
<term>Experimental conditions</term>
<term>Feb</term>
<term>Febs lett</term>
<term>Final reaction products</term>
<term>Incubation time</term>
<term>Ionic strength</term>
<term>Klenow fragment</term>
<term>Labelling experiments</term>
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<term>Mung bean nuclease</term>
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<term>Nicking activity</term>
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<term>Nucleic</term>
<term>Nucleic acids</term>
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<term>Phytolacca dioica</term>
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<term>Preferential cleavage site</term>
<term>Proof nicking</term>
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<term>Purification procedure</term>
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<term>Rrna</term>
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<term>Standard conditions</term>
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<front><div type="abstract" xml:lang="en">Ribosome-inactivating proteins isolated from Phytolacca dioica L. leaves are rRNA-N-glycosidases, as well as adenine polynucleotide glycosylases. Here we report that some of them cleave supercoiled pBR322 dsDNA, generating relaxed and linear molecules. PD-L1, the glycosylated major form isolated from the winter leaves of adult P. dioica plants, produces both free 3′-OH and 5′-P termini randomly distributed along the DNA molecule, as suggested by labelling experiments with [α-32P]dCTP and [γ-32P]dATP. Moreover, when the reaction is carried out under low-salt conditions, cleavage is observed mainly at a specific site, located downstream of the ampicillin resistance gene (close to position 3200), ending with the deletion of a fragment of approximately 70 nucleotides. This cleavage pattern is similar to that obtained under the same conditions with mung bean nuclease, a single-strand endonuclease. Furthermore, pBR322 DNA treated with PD-L1 shows reduced transforming activity with E. coli HB101 competent cells in comparison to untreated control plasmid DNA.</div>
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Nicking activity on pBR322 DNA of ribosome inactivating proteins from Phytolacca dioica L. leaves

Nicking activity on pBR322 DNA of ribosome inactivating proteins from Phytolacca dioica L. leaves

Source :

English descriptors

Abstract

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